8QQC
Crystal structure of Lymantria dispar CPV14 polyhedra single crystal
Summary for 8QQC
| Entry DOI | 10.2210/pdb8qqc/pdb |
| Descriptor | Polyhedrin, GUANOSINE-5'-TRIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | polyhedrin, gtp binding, viral protein |
| Biological source | Lymantria dispar (gypsy moth) |
| Total number of polymer chains | 1 |
| Total formula weight | 29270.93 |
| Authors | Trincao, J.,Warren, A.,Crawshaw, A.,Sutton, G.,Stuart, D.,Evans, G. (deposition date: 2023-10-04, release date: 2023-11-08, Last modification date: 2024-11-20) |
| Primary citation | Warren, A.J.,Trincao, J.,Crawshaw, A.D.,Beale, E.V.,Duller, G.,Stallwood, A.,Lunnon, M.,Littlewood, R.,Prescott, A.,Foster, A.,Smith, N.,Rehm, G.,Gayadeen, S.,Bloomer, C.,Alianelli, L.,Laundy, D.,Sutter, J.,Cahill, L.,Evans, G. VMXm - A sub-micron focus macromolecular crystallography beamline at Diamond Light Source. J.Synchrotron Radiat., 31:1593-1608, 2024 Cited by PubMed Abstract: VMXm joins the suite of operational macromolecular crystallography beamlines at Diamond Light Source. It has been designed to optimize rotation data collections from protein crystals less than 10 µm and down to below 1 µm in size. The beamline has a fully focused beam of 0.3 × 2.3 µm (vertical × horizontal) with a tuneable energy range (6-28 keV) and high flux (1.6 × 10 photons s at 12.5 keV). The crystals are housed within a vacuum chamber to minimize background scatter from air. Crystals are plunge-cooled on cryo-electron microscopy grids, allowing much of the liquid surrounding the crystals to be removed. These factors improve the signal-to-noise during data collection and the lifetime of the microcrystals can be prolonged by exploiting photoelectron escape. A novel in vacuo sample environment has been designed which also houses a scanning electron microscope to aid with sample visualization. This combination of features at VMXm allows measurements at the physical limits of X-ray crystallography on biomacromolecules to be explored and exploited. PubMed: 39475835DOI: 10.1107/S1600577524009160 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.3 Å) |
Structure validation
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